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Full-Text Articles in Nutrition
New Guidelines For Assessment Of Malnutrition In Adults: Obese Clinically Ill Patients, Kasuen Mauldin, Colleen O'Leary-Kelley
New Guidelines For Assessment Of Malnutrition In Adults: Obese Clinically Ill Patients, Kasuen Mauldin, Colleen O'Leary-Kelley
Kasuen Mauldin
No abstract provided.
The Carboxyl-Terminal Segment Of Apolipoprotein A-V Undergoes A Lipid-Induced Conformational Change, Kasuen Mauldin, B. L. Lee, M. Oleszczuk, B. D. Sykes, R. O. Ryan
The Carboxyl-Terminal Segment Of Apolipoprotein A-V Undergoes A Lipid-Induced Conformational Change, Kasuen Mauldin, B. L. Lee, M. Oleszczuk, B. D. Sykes, R. O. Ryan
Kasuen Mauldin
Apolipoprotein (apo) A-V is a 343-residue, multidomain protein that plays an important role in regulation of plasma triglyceride homeostasis. Primary sequence analysis revealed a unique tetraproline sequence (Pro293-Pro296) near the carboxyl terminus of the protein. A peptide corresponding to the 48-residue segment beyond the tetraproline motif was generated from a recombinant apoA-V precursor wherein Pro295 was replaced by Met. Cyanogen bromide cleavage of the precursor protein, followed by negative affinity chromatography, yielded a purified peptide. Nondenaturing polyacrylamide gel electrophoresis verified that apoA-V(296-343) solubilizes phospholipid vesicles, forming a relatively heterogeneous population of reconstituted high-density lipoprotein with Stokes’ diameters>17 nm. At …
The N-Terminus Of Apolipoprotein A-V Adopts A Helix-Bundle Molecular Architecture, Kasuen Wong, J. A. Beckstead, D. Lee, P. M.M. Weers, E. Guigard, C. M. Kay, R. O. Ryan
The N-Terminus Of Apolipoprotein A-V Adopts A Helix-Bundle Molecular Architecture, Kasuen Wong, J. A. Beckstead, D. Lee, P. M.M. Weers, E. Guigard, C. M. Kay, R. O. Ryan
Kasuen Mauldin
Previous studies of recombinant full-length human apolipoprotein A-V (apoA-V) provided evidence of the presence of two independently folded structural domains. Computer-assisted sequence analysis and limited proteolysis studies identified an N-terminal fragment as a candidate for one of the domains. C-Terminal truncation variants in this size range, apoA-V(1-146) and apoA-V(1-169), were expressed in Escherichia coli and isolated. Unlike full-length apoA-V or apoA-V(1-169), apoA-V(1-146) was soluble in neutral-pH buffer in the absence of lipid. Sedimentation equilibrium analysis yielded a weight-average molecular weight of 18811, indicating apoA-V(1-146) exists as a monomer in solution. Guanidine HCl denaturation experiments at pH 3.0 yielded a one-step …